| Definition | Desulfotomaculum reducens MI-1 chromosome, complete genome. |
|---|---|
| Accession | NC_009253 |
| Length | 3,608,104 |
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The map label for this gene is ribH
Identifier: 134299936
GI number: 134299936
Start: 2286172
End: 2286636
Strand: Reverse
Name: ribH
Synonym: Dred_2090
Alternate gene names: 134299936
Gene position: 2286636-2286172 (Counterclockwise)
Preceding gene: 134299937
Following gene: 134299934
Centisome position: 63.38
GC content: 44.3
Gene sequence:
>465_bases ATGCCGAAAGTATTTGAAGGACATTTACTGGGACAAGAATTAAAGTTTGGTATTGTTGTTGGTCGTTTTAACGAATTTAT TACTAATAAATTGTTAAGCGGAGCACTAGATGCCTTGAAACGTCATGGCGTAGAGGACGAAAATGTTGAAATTGCTTATG TTCCCGGGGCCTATGAAATTCCTTTGGTGGCAAAGAAAATGGCTGATAGCAAACGTTACGATGGCGTTATTTGCTTGGGG GCGGTAATTCGTGGCGCAACCCCTCACTTTGAATACGTATCAGCGGAAGTTTCCAAAGGGGTGGCAAAGATCAGTTTGGA TAGCAATCTGCCGGTGATCTTTGGCGTACTGACCGTAGATACCATCGAACAGGCCATCGAGCGGGCTGGTACCAAGGCTG GCAACAAAGGTTGGGAAGCTGCCAATGCTGCCATTGAAATGGCCAATTTATTAAAAACTATCTAG
Upstream 100 bases:
>100_bases AAATGCAAACTGGGTCATCTTTTAACCCTGGAAGAAAAGTCTAAGAAATCGGTCAATGAATAAAATCATTACGAATTATA AGTAACAGGAGGACAAAAAT
Downstream 100 bases:
>100_bases GAAAAACACTAAGAAAACCCGGAATTTTTCCGGGTTTTCTTAGTTTATCAAAAGTATTTAAGTTTTCGATACAATTGATG CCTGGGTCAGGGCAAATAAA
Product: riboflavin synthase
Products: NA
Alternate protein names: DMRL synthase; Lumazine synthase; Riboflavin synthase beta chain
Number of amino acids: Translated: 154; Mature: 153
Protein sequence:
>154_residues MPKVFEGHLLGQELKFGIVVGRFNEFITNKLLSGALDALKRHGVEDENVEIAYVPGAYEIPLVAKKMADSKRYDGVICLG AVIRGATPHFEYVSAEVSKGVAKISLDSNLPVIFGVLTVDTIEQAIERAGTKAGNKGWEAANAAIEMANLLKTI
Sequences:
>Translated_154_residues MPKVFEGHLLGQELKFGIVVGRFNEFITNKLLSGALDALKRHGVEDENVEIAYVPGAYEIPLVAKKMADSKRYDGVICLG AVIRGATPHFEYVSAEVSKGVAKISLDSNLPVIFGVLTVDTIEQAIERAGTKAGNKGWEAANAAIEMANLLKTI >Mature_153_residues PKVFEGHLLGQELKFGIVVGRFNEFITNKLLSGALDALKRHGVEDENVEIAYVPGAYEIPLVAKKMADSKRYDGVICLGA VIRGATPHFEYVSAEVSKGVAKISLDSNLPVIFGVLTVDTIEQAIERAGTKAGNKGWEAANAAIEMANLLKTI
Specific function: Riboflavin synthase is a bifunctional enzyme complex catalyzing the formation of riboflavin from 5-amino-6-(1'-D)- ribityl-amino-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydrohy-2- butanone-4-phosphate via 6,7-dimethyl-8-lumazine. The beta subunit catalyzes
COG id: COG0054
COG function: function code H; Riboflavin synthase beta-chain
Gene ontology:
Cell location: Cytoplasm [C]
Metaboloic importance: Non_Essential [C]
Operon status: Not Known
Operon components: None
Similarity: Belongs to the DMRL synthase family
Homologues:
Organism=Escherichia coli, GI1786617, Length=153, Percent_Identity=55.5555555555556, Blast_Score=173, Evalue=6e-45, Organism=Saccharomyces cerevisiae, GI6324429, Length=147, Percent_Identity=38.0952380952381, Blast_Score=101, Evalue=5e-23,
Paralogues:
None
Copy number: NA
Swissprot (AC and ID): RISB_DESRM (A4J6A4)
Other databases:
- EMBL: CP000612 - RefSeq: YP_001113432.1 - ProteinModelPortal: A4J6A4 - SMR: A4J6A4 - STRING: A4J6A4 - GeneID: 4955321 - GenomeReviews: CP000612_GR - KEGG: drm:Dred_2090 - eggNOG: COG0054 - HOGENOM: HBG311126 - OMA: KAGNKGW - PhylomeDB: A4J6A4 - BioCyc: DRED349161:DRED_2090-MONOMER - HAMAP: MF_00178 - InterPro: IPR002180 - Gene3D: G3DSA:3.40.50.960 - PANTHER: PTHR21058 - TIGRFAMs: TIGR00114
Pfam domain/function: PF00885 DMRL_synthase; SSF52121 DMRL_synthase
EC number: =2.5.1.9
Molecular weight: Translated: 16570; Mature: 16439
Theoretical pI: Translated: 6.27; Mature: 6.27
Prosite motif: NA
Important sites: NA
Signals:
None
Transmembrane regions:
None
Cys/Met content:
0.6 %Cys (Translated Protein) 1.9 %Met (Translated Protein) 2.6 %Cys+Met (Translated Protein) 0.7 %Cys (Mature Protein) 1.3 %Met (Mature Protein) 2.0 %Cys+Met (Mature Protein)
Secondary structure:
>Translated Secondary Structure MPKVFEGHLLGQELKFGIVVGRFNEFITNKLLSGALDALKRHGVEDENVEIAYVPGAYEI CCCCCCCCCCCCHHHHEEEEHHHHHHHHHHHHHHHHHHHHHCCCCCCCEEEEECCCCCCC PLVAKKMADSKRYDGVICLGAVIRGATPHFEYVSAEVSKGVAKISLDSNLPVIFGVLTVD HHHHHHHHCCCCCCCEEEEHHHHHCCCCCHHHHHHHHHCCEEEEEECCCCCEEEHHHHHH TIEQAIERAGTKAGNKGWEAANAAIEMANLLKTI HHHHHHHHHCCCCCCCCHHHHHHHHHHHHHHHCC >Mature Secondary Structure PKVFEGHLLGQELKFGIVVGRFNEFITNKLLSGALDALKRHGVEDENVEIAYVPGAYEI CCCCCCCCCCCHHHHEEEEHHHHHHHHHHHHHHHHHHHHHCCCCCCCEEEEECCCCCCC PLVAKKMADSKRYDGVICLGAVIRGATPHFEYVSAEVSKGVAKISLDSNLPVIFGVLTVD HHHHHHHHCCCCCCCEEEEHHHHHCCCCCHHHHHHHHHCCEEEEEECCCCCEEEHHHHHH TIEQAIERAGTKAGNKGWEAANAAIEMANLLKTI HHHHHHHHHCCCCCCCCHHHHHHHHHHHHHHHCC
PDB accession: NA
Resolution: NA
Structure class: Unstructured
Cofactors: NA
Metal ions: NA
Kcat value (1/min): NA
Specific activity: NA
Km value (mM): NA
Substrates: NA
Specific reaction: NA
General reaction: NA
Inhibitor: NA
Structure determination priority: 10.0
TargetDB status: NA
Availability: NA
References: NA